5OLO
Structure of the A2A-StaR2-bRIL562-Tozadenant complex at 3.1A obtained from in meso soaking experiments.
Summary for 5OLO
| Entry DOI | 10.2210/pdb5olo/pdb |
| Descriptor | Adenosine receptor A2a,Soluble cytochrome b562,Adenosine receptor A2a, ~{N}-(4-methoxy-7-morpholin-4-yl-1,3-benzothiazol-2-yl)-4-methyl-4-oxidanyl-piperidine-1-carboxamide, CHOLESTEROL, ... (7 entities in total) |
| Functional Keywords | g-protein coupled receptor, adenosine 2a receptor, 7 tm integral membrane protein, thermostabilizing mutations, membrane protein |
| Biological source | Homo sapiens (Human) More |
| Cellular location | Cell membrane; Multi-pass membrane protein: P29274 |
| Total number of polymer chains | 1 |
| Total formula weight | 55334.21 |
| Authors | Rucktooa, P.,Cheng, R.K.Y.,Segala, E.,Geng, T.,Errey, J.C.,Brown, G.A.,Cooke, R.,Marshall, F.H.,Dore, A.S. (deposition date: 2017-07-28, release date: 2018-01-17, Last modification date: 2024-10-16) |
| Primary citation | Rucktooa, P.,Cheng, R.K.Y.,Segala, E.,Geng, T.,Errey, J.C.,Brown, G.A.,Cooke, R.M.,Marshall, F.H.,Dore, A.S. Towards high throughput GPCR crystallography: In Meso soaking of Adenosine A2A Receptor crystals. Sci Rep, 8:41-41, 2018 Cited by PubMed Abstract: Here we report an efficient method to generate multiple co-structures of the A G protein-coupled receptor (GPCR) with small-molecules from a single preparation of a thermostabilised receptor crystallised in Lipidic Cubic Phase (LCP). Receptor crystallisation is achieved following purification using a low affinity "carrier" ligand (theophylline) and crystals are then soaked in solutions containing the desired (higher affinity) compounds. Complete datasets to high resolution can then be collected from single crystals and seven structures are reported here of which three are novel. The method significantly improves structural throughput for ligand screening using stabilised GPCRs, thereby actively driving Structure-Based Drug Discovery (SBDD). PubMed: 29311713DOI: 10.1038/s41598-017-18570-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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